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    Changes in lipid membranes may trigger amyloid toxicity in Alzheimer's disease

    Year: 2017

    Journal: PLoS One, Volume 12, AUG 2

    Authors: Drolle, Elizabeth; Negoda, Alexander; Hammond, Keely; Pavlov, Evgeny; Leonenko, Zoya

    Organizations: Natural Science and Engineering Council of Canada (NSERC); Heart and Stroke Foundation of Canada grant; American Heart Association; WIN; NSERC

    Amyloid-beta peptides (A beta), implicated in Alzheimer's disease (AD), interact with the cellular membrane and induce amyloid toxicity. The composition of cellular membranes changes in aging and AD. We designed multi-component lipid models to mimic healthy and diseased states of the neuronal membrane. Using atomic force microscopy (AFM), Kelvin probe force microscopy (KPFM) and black lipid membrane (BLM) techniques, we demonstrated that these model membranes differ in their nanoscale structure and physical properties, and interact differently with A beta(1-42). Based on our data, we propose a new hypothesis that changes in lipid membrane due to aging and AD may trigger amyloid toxicity through electrostatic mechanisms, similar to the accepted mechanism of antimicrobial peptide action. Understanding the role of the membrane changes as a key activating amyloid toxicity may aid in the development of a new avenue for the prevention and treatment of AD.
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